BMRB Entry 7205

Name: 1H, 13C, and 15N Chemical Shift Assignments for Transmembrane Segment of ErbB4
Published: 2007-01-09

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PDB ID: 2lcx
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR7205
MolProbity Validation Chart

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Nicholas Rego and David Koes
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

1H, 13C, and 15N Chemical Shift Assignments for Transmembrane Segment of ErbB4

Deposition date:

2006-07-03

Original release date:

2007-01-09

Authors:

Mineev, Konstantin; Bocharov, Eduard; Maslennikov, Innokenty; Goncharuk, Marina; Arseniev, Alexander

Citation:

Citation: Bocharov, Eduard; Mineev, Konstantin; Volynsky, Pavel; Ermolyuk, Y.; Tkach, E.; Sobol, A.; Chupin, V.; Kirpichnikov, M.; Efremov, R.; Arseniev, Alexander. "Spatial structure of the dimeric transmembrane domain of the growth factor receptor ErbB2 presumably corresponding to the receptor active state" J. Biol. Chem. 283, 6950-6956 (2008).
PubMed: 18178548

Assembly members:

Assembly members:
ErbB4 TM, polymer, 44 residues, 4760 Da.

Natural source:

Natural source: Common Name: Human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo spaiens

Experimental source:

Experimental source: Production method: recombinant technology

Entity Sequences (FASTA):

Entity Sequences (FASTA):
ErbB4 TM: STLPQHARTPLIAAGVIGGL FILVIVGLTFAVYVRRKSIK KKRA

Data sets:

assigned_chemical_shifts
- chem_shift_list_1
coupling_constants
- J_coupling_list_1
heteronucl_T1_relaxation
- T1_list_1
heteronucl_T2_relaxation
- T2_list_1

Data type	Count
13C chemical shifts	179
15N chemical shifts	40
1H chemical shifts	316
coupling constants	37
T1 relaxation values	36
T2 relaxation values	34

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	ErbB4 TM, chain 1	1
2	ErbB4 TM, chain 2	2

Entities:

Entity 1, ErbB4 TM, chain 1 44 residues - 4760 Da.

1

SER

THR

LEU

PRO

GLN

HIS

ALA

ARG

THR

PRO

2

LEU

ILE

ALA

GLY

VAL

ILE

GLY

LEU

3

PHE

ILE

LEU

VAL

ILE

VAL

GLY

LEU

THR

PHE

4

ALA

VAL

TYR

VAL

ARG

LYS

SER

ILE

LYS

5

LYS

ARG

ALA

Entity 2, ErbB4 TM, chain 2 44 residues - 4760 Da.

1

SER

THR

LEU

PRO

GLN

HIS

ALA

ARG

THR

PRO

2

LEU

ILE

ALA

GLY

VAL

ILE

GLY

LEU

3

PHE

ILE

LEU

VAL

ILE

VAL

GLY

LEU

THR

PHE

4

ALA

VAL

TYR

VAL

ARG

LYS

SER

ILE

LYS

5

LYS

ARG

ALA

Samples:

sample_1: ErbB4 TM, [U-15N], 2.4 ± 0.3 mM; DMPC, [U-2H], 19 ± 1 mM; DHPC, [U-2H], 77 ± 1 mM

sample_2: ErbB4 TM, [U-15N; U-13C], 2.4 ± 0.3 mM; DMPC, [U-2H], 19 ± 1 mM; DHPC, [U-2H], 77 ± 1 mM

sample_3: ErbB4 TM, [U-15N; U-13C], 0.6 ± 0.3 mM; DMPC, [U-2H], 19 ± 1 mM; DHPC, [U-2H], 77 ± 1 mM; ErbB4 TM, none, 0.6 ± 0.3 mM

conditions_1: pH: 5.0; temperature: 313 K

Experiments:

Name	Sample	Sample state	Sample conditions
1H15N HSQC	not available	not available	conditions_1
1H13C HSQC	not available	not available	conditions_1
HCcH-TOCSY	not available	not available	conditions_1
3D 13C-ali NOESY	not available	not available	conditions_1
3D 15N-NOESY	not available	not available	conditions_1
3D 15N-TOCSY	not available	not available	conditions_1
HNCA	not available	not available	conditions_1
HN(CO)CA	not available	not available	conditions_1
HNCO	not available	not available	conditions_1
HNHA	not available	not available	conditions_1
HNHB	not available	not available	conditions_1
2D NC-chirp-NOESY	not available	not available	conditions_1
3D C-chirp-NOESY	not available	not available	conditions_1

Software:

VNMR -

NMR spectrometers:

Varian Unity 600 MHz

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks